Home LiteratureArticle Details
PMID: 4230510 Published · ppublish English Journal Article

Tritiated digoxin binding to (Na+ + K+)-activated adenosine triphosphatase: possible allosteric site.

Science (New York, N.Y.) ·Vol. 160 ·No. 3825 ·1968-04-19 ·Pages 323-5

Schwartz A, Matsui H, Laughter AH

Abstract

Tritiated H(3)-digoxin specifically binds to a cardiac (Na(+) + K(+))-activated adenosine triphosphatase. In the presence of adenosine triphosphate and other nucleoside di- and triphosphates, binding is stimulated by sodium ion, the apparent rate constant being similar to that reported for phosphorus-32 incorporation from adenosine triphosphate and for the adenosine triphosphatase activity. In the presence of magnesium, manganese, inorganic phosphate, or other ions, sodium ion inhibits binding. The data support an allosteric type of sodium-potassium ion pump.

MeSH Terms
Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Animals Binding Sites Biological Transport, Active Cattle Digoxin/metabolism Magnesium/pharmacology Manganese/pharmacology Myocardium/enzymology Phosphates/pharmacology Potassium/pharmacology Sodium/pharmacology Tritium
Chemicals
Phosphates Tritium Manganese Digoxin Adenosine Triphosphate Sodium Adenosine Triphosphatases Magnesium Potassium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Schwartz A
Matsui H
Laughter A H
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1968-04-19
Pages
323-5
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]